Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A cell hybrid has been selected from fusion of a mouse myeloma and rat spleen cells immunized against mouse lymphoma cells that produces monoclonal antibody against the mouse lymphocyte surface glycoprotein, T200. Antibody binding assays employing the monoclonal antibody show that there are about 50,000-100,000 molecules of T200 glycoprotein on mouse thymocytes and that similar antigens are present on spleen and bone marrow but not detected on nonlymphoid tissues. Examination of the labeled molecules precipitated from detergent extracts of spleen cells and thymocytes iodinated by the lactoperoxidase technique by SDS-PAGE confirm that there are structural differences between the antigens found on B and T lymphocytes. The B-cell glycoprotein consists of at least one component of apparent mol wt 220,000 on SDS-PAGE, while the T-cell glycoprotein has an apparent mol wt of about 190,000.
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PMID:Interspecies spleen-myeloma hybrid producing monoclonal antibodies against mouse lymphocyte surface glycoprotein, T200. 7 61

Human and mouse lymphocytes were surface-labeled by lactoperoxidase-catalyzed iodination, or by galactose oxidase oxidation followed by reduction with tritiated sodium borohydride. The labeled cells were lysed with Nonidet P-40. Proteins binding to Helix pomatia A hemagglutinin (HP) were isolated by affinity chromatography on HP-Sepharose and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography. A major cell surface glycoprotein (apparent mol. wt. 150 000, using reducing conditions) on human lymphocytes was responsible for almost all binding of HP. This protein was present on normal and malignant thymus-derived lymphocytes, e.g. thymocytes, blood T cells and T leukemia cell lines. It was also found on chronic lymphocytic leukemia cells, one null cell leukemia line, one unidentified leukemia line, one lymphoblastoid cell line of B origin and on one stem cell lymphoma line. In contrast, this protein was not found on various B cells at different steps of differentiation, e.g. four B lymphoma lines or one myeloma line. It was also absent from a histiocytic leukemia line. However, two of the four B lymphoma lines and the myeloma line had another HP-binding surface glycoprotein (mol. wt. 200 000) instead of the 150 000 protein. Studies of mouse lymphocytes similarly showed that thymus-derived lymphocytes (normal and malignant) but not normal adult B cells expressed a major HP-binding surface glycoprotein of apparent mol. wt. 130 000 (reducing conditions).
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PMID:Helix pomatia A hemagglutinin: selectivity of binding to lymphocyte surface glycoproteins on T cells and certain B cells. 30 19

Two different methods, immunofluorescence and lactoperoxidase-catalysed radioiodination, were used to investigate mIg on two different myeloma cell lines. The data indicate that, even though both techniques are highly sensitive, different results can be obtained in the same cell line depending on the technique employed.
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PMID:Membrane immunoglobulin on mouse myeloma cells: discrepancies in the detection of membrane IG by two different methods. 76 90

A human-mouse hybridoma has been produced by fusion of Hashimoto thyroid lymphocytes with the mouse myeloma line X63-Ag8.653. The cloned hybridoma secreted 2.5 micrograms per 10(6) cells per day of an IgG kappa thyroid peroxidase (TPO) autoantibody (2G4) with high affinity (2.5 x 10(9) molar-1) and specificity for human TPO. 2G4 did not react with lactoperoxidase, horseradish peroxidase or human myeloperoxidase or with porcine TPO or with human thyroglobulin. Plastic tubes coated with 2G4 bound about 50% of 125I-labelled human TPO added and the binding was inhibited by IgGs prepared from 18/18 TPO autoantibody-positive sera. This indicated that all 18 sera contained autoantibodies which recognised the same (or closely related) epitope as 2G4. Plastic tubes coated with IgGs from different TPO autoantibody-positive patient sera also bound 125I-labelled TPO but inhibition by 2G4 in this system was not complete. This suggested that the sera contained at least 2 types of TPO autoantibodies, with only one type of autoantibody reactive with the same epitope as 2G4.
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PMID:Production and characterisation of a human monoclonal thyroid peroxidase autoantibody. 128 77

Autologous (Heymann) nephritis was induced by immunizing Sprague-Dawley rats with a crude membrane extract (Fx1A) prepared from renal cortical tubules. Urine protein excretion was monitored to determine the onset of nephritis and then the spleens of nephritic rats were fused with a non-secretor rat myeloma cell line. Supernatants from hybridoma cultures were first screened for production of anti-brush border membrane (BBM) antibody by immunodot blotting of highly purified rat BBM on nitrocellulose. Positive hybrids were then tested by indirect immunofluorescence for the presence of IgG, which binds to the brush border of rat renal proximal tubules. Those hybrids which were positive by both screening assays were subcloned twice. Two monoclonal antibodies (C5, D11) were studied in some detail. Both C5 and D11 immunoprecipitated a single polypeptide from BBM, labelled with 125I by the lactoperoxidase method. Radioautography of gradient 4-11% slab sodium dodecyl sulphate polyacrylamide gels revealed that the polypeptide against which C5 and D11 were directed co-migrated with the polypeptide immunoprecipitated by (i) IgG eluted from the renal cortex of nephritic rats, and by (ii) a mouse anti-rat monoclonal against gp 330 [a BBM constituent with proven pathogenicity [9]]. Supernatants which tested positive by immunodot blotting but negative by indirect immunofluorescence showed no detectable immunoprecipitate after reaction with BBM. Immunocytochemical staining by immunoperoxidase and immunogold methods localized C5 and D11 to the BBM of the renal proximal tubule and to the urine face of the glomerular epithelium.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A rat hybridoma model of Heymann nephritis: production of a monoclonal anti GP330 from a nephritic rat. 227 21

Peripheral blood mononuclear cells from a patient with chronic myelogenous leukemia (CML), in remission, were depleted of CD8-positive T-cells and cultured with Epstein-Barr virus. Four of 20 cultures (20%) secreted human IgG antibodies selectively reactive with the cell surfaces of certain human leukemia cell lines. Three polyclonal, Epstein-Barr virus-transformed, B-cell lines were expanded and fused with the human-mouse myeloma analogue HMMA2.11TG/O. Antibody from secreting clones HL 1.2 (IgG1), HL 2.1 (IgG3), and HL 3.1 (IgG1) have been characterized. All three react with HL-60 (promyelocytic), RWLeu4 (CML promyelocytic), and U937 (monocytic), but not with KG-1 (myeloblastic) or K562 (CML erythroid). There is no reactivity with T-cell lines, Burkitt's cell lines, pre-B-leukemia cell lines, or an undifferentiated CML cell line, BV173. Leukemic cells from two of seven patients with acute myelogenous leukemia and one of five with acute lymphocytic leukemia react with all three antibodies. Normal lymphocytes, monocytes, polymorphonuclear cells, red blood cells, bone marrow cells, and platelets do not react. Samples from patients with other diverse hematopoietic malignancies showed no reactivity. Immunoprecipitations suggest that the reactive antigen(s) is a lactoperoxidase iodinatable series of cell surface proteins with molecular weights of 42,000-54,000 and a noniodinatable protein with a molecular weight of 82,000. Based on these data these human monoclonal antibodies appear to react with myelomonocytic leukemic cells and may detect a leukemia-specific antigen or a highly restricted differentiation antigen.
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PMID:Human monoclonal antibodies reactive with human myelomonocytic leukemia cells. 292 15

We have assessed the tumoricidal potential of enzyme-antibody conjugates on murine myeloma cells. Conjugates of glucose oxidase (EC 1.1.3.4) and lactoperoxidase (EC 1.11.1.7) were specifically targeted on the NSO tumor cells. Optimal conditions for tumor cell killing, as assayed by [51Cr] release required the binding of both antibody conjugates to the cell membrane. This is followed by washing and incubation in medium containing glucose and 0.1 mM iodide. Under these conditions 90% of the incorporated [51Cr] labeled is released from the cells, and NSO clonogenicity is reduced by a factor greater than 5 logs by 2 h of incubation.
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PMID:In-vitro cytolysis of myeloma tumor cells with glucose oxidase and lactoperoxidase antibody conjugates. 376 10

In an effort to develop new approaches to the study and control of infectious diarrhea, we prepared murine monoclonal antibodies to the Escherichia coli heat-stable enterotoxin (STa). The toxin was purified from E. coli culture media and conjugated to bovine serum albumin. The STa-bovine serum albumin conjugate was used to immunize BALB/c mice, and the immune spleen cells from these mice were fused with SP2/0 myeloma cells. Resultant hybridomas were screened in an enzyme-linked immunosorbent assay protocol against 500 ng of STa-bovine serum albumin bound to microtiter wells as the solid-phase antigen. Five stable clones were selected and grown further in ascites fluid, which demonstrated anti-STa activity at dilutions of up to 1:500,000 in the enzyme-linked immunosorbent assay for heat-stable enterotoxin. In a competitive enzyme-linked immunosorbent assay format, the antibodies recognized several human and porcine strains of STa to various extents, but did not recognize E. coli heat-labile toxin, cholera toxin, or staphylococcal enterotoxin B. The antibodies were all able to bind lactoperoxidase-labeled [125I]STa, and antibody 20B3 was also able to dissociate [125I]STa bound to toxin receptors on rat jejunal villous cells. Preincubation of STa with antibodies 20B3 or 20F5 led to a concentration-dependent neutralization of toxin activity in a suckling mouse intestinal secretion assay. These antibodies are likely to provide new tools for the continued study of STa structure-function relationships and may lead to improved diagnosis and treatment of E. coli-induced infectious diarrhea.
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PMID:Production of neutralizing monoclonal antibodies to Escherichia coli heat-stable enterotoxin. 388 Jul 23

Eight monoclonal antibodies (MAbs) raised against human prostate cancer cell lines are described. One MAb was derived from the fusion of mouse myeloma P3x63Ag8-653 cells with spleen cells of mice immunized with DU145 prostate cancer cells. The other seven were from the fusion of myeloma lines P3x63Ag8-653 or SP2/0 with spleen cells of mice immunized with PC3, DU145 and 1013L prostate cancer cells. All of the antibodies also reacted with cell lines of other human cancer types, especially carcinomas. Immunoperoxidase staining on fixed tissue revealed strong reactivity only with antibody PrN10. Seven other antibodies seemed to bind to cell surface-associated (glyco)proteins. Antibodies PrL22 and PrO11 showed similar reactivity in radioimmunoassay, and immunoprecipitated a 160 kD molecular weight polypeptide from [125I]lactoperoxidase-labeled cells. Antibodies PrHk an PrQ12 bound to molecules with apparent MW of 115 kD and 100 kD, respectively; antibodies PrM24 and PrP14 revealed a more complex picture in immunoprecipitation of surface-labeled cells.
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PMID:Shared antigens of human prostate cancer cell lines as defined by monoclonal antibodies. 388 36

kappa-Myeloma antigen (KMA) was immunoprecipitated from lactoperoxidase-radioiodinated HMy2 lymphoblastoid cells by using monoclonal antibody K-1-21 and was analyzed by SDS-PAGE. Under reducing conditions, two major subunits of Mr approximately 26,000 and Mr approximately 42,000, and minor components of Mr approximately 28,000, 31,000, and 36,000 were observed. The Mr approximately 26,000 subunit was identical to kappa-light chains from HMy2 surface IgG in apparent m.w., isoelectric point, and staphylococcal V-8 protease peptide map, but was not precipitated in association with Ig heavy chain. The Mr approximately 42,000 component was homologous to rabbit skeletal muscle actin by peptide mapping with staphylococcal V-8 protease. The cell surface origin of the immunoprecipitated antigen was confirmed by demonstrating lactoperoxidase dependence of iodination and complete removal from the cell surface after pronase treatment of viable cells. Thus, cell surface expression of KMA is the result of membrane association of non-heavy chain-linked kappa-light chains, possibly in noncovalent association with actin.
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PMID:Structural analysis of the myeloma-associated membrane antigen KMA. 392 6


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